Selective Inhibition by Sodium Butyrate of Glucorticoid‐Induced Tyrosine Aminotransferase Synthesis in Hepatoma Tissue‐Cultured Cells

Tichonicky, Lydie; Santana, María Angélica; Defer, Nicole; Giesen, Eva Maria; Beck, G.; Kruh, Jacques

doi:10.1111/j.1432-1033.1981.tb05720.x

Cited by 34 publications

(10 citation statements)

References 53 publications

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“…Interestingly, the amplified or transfected gene is still inducible by heavy metals. Butyrate, which inhibits histone deacetylase (but also histone acetyltransferase) and alters chromatin structure, reversibly reduces the accumulation of tyrosine aminotransferase mRNA seen in response to glucocorticoids, without affecting the basal levels (Tichonicky et al, 1981). Plesko et al (1983) have shown that this short-term inhibitory effect of butyrate on transcription is specific for a few mRNA species, most of which are glucocorticoidinducible.…”

Section: Involvement Of Chromatinmentioning

confidence: 99%

Control of gene expression by glucocorticoid hormones

Rousseau¹

1984

Biochemical Journal

142

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Glucocorticoids control the expression of a small number of transcriptionally active genes by increasing or decreasing mRNA concentration. Either effect can result from a transcriptional or a post-transcriptional mechanism. Induction of mouse mammary tumour virus RNA results from a stimulation of transcription initiation and depends on the presence of defined regions in proviral DNA. These regions bind the glucocorticoid receptor and behave functionally as proto-enhancers. Glucocorticoid-inducible genes can retain their sensitivity to the hormone after transfer to a heterologous cell by transfection techniques. Non-inducible genes can become inducible when linked to the promoter region of an inducible gene. The mechanisms by which the receptor-steroid complex stimulates or inhibits transcription or influences mRNA stability are unknown. Receptor binding to nucleic acids appears to be a necessary but not sufficient condition. It is likely that the receptor also interacts with chromatin proteins. This might lead to a catalytic modification of these proteins, resulting in a modulation of gene expression. Development of glucocorticoid-sensitive, biochemically defined, cell-free transcription systems should provide a tool to delineate the molecular determinants of this essential regulatory mechanism.

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Section: Involvement Of Chromatinmentioning

confidence: 99%

Control of gene expression by glucocorticoid hormones

Rousseau¹

1984

Biochemical Journal

142

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“…Butyrate and glucocorticoids have antagonistic effects in a number of cell lines. Thus, butyrate prevents gene induction by glucocorticoids in glioma and hepatoma cells and inhibits activation by glucocorticoids of murine mammary tumor virus genes in other cells lines, whereas dexamethasone blocks the butyrate-induced differentiation of rat islet cells (2,25,32,33). Since ␣-ABA decreases the rate of globin gene switching in the hybrids, we wished to test whether glucocorticoids would have the opposite effect, i.e., acceleration of the ␥-to-␤ switch.…”

Section: Resultsmentioning

confidence: 99%

“…Butyrate and its analogs are well-established inducers or repressors of differentiation in various cellular systems (2,4,15,16,17,25,26,28,32,33). The mechanism whereby these compounds affect gene expression remains unresolved; however, it is assumed that effects on gene expression may be mediated by histone hyperacetylation because of the inhibition of histone deacetylase (17,31).…”

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confidence: 99%

Effects of Butyrate and Glucocorticoids on γ- to β-Globin Gene Switching in Somatic Cell Hybrids

Zitnik

Peterson

Stamatoyannopoulos

et al. 1995

Molecular and Cellular Biology

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Butyrate and its analogs have been shown to induce fetal hemoglobin in humans and primates and in erythroid cell cultures. To obtain insights concerning the cellular mechanisms of butyrate action, we analyzed the effects of butyrate on human globin gene expression in hybrids produced by fusing mouse erythroleukemia cells (MEL) with human fetal erythroid cells (HFE). These hybrids initially express human fetal hemoglobin but subsequently switch to adult globin expression after several weeks in culture. We found that ␣-aminobutyric acid, a butyrate analog which does not induce terminal maturation, strikingly delays the rate of the ␥-to ␤-globin gene (␥-to-␤) switch in the HFE ؋ MEL hybrids. The effect of butyrate on globin expression is transient, with the result that the delay of globin gene switching requires the continuous presence of this compound in culture. Furthermore, butyrate fails to induce fetal hemoglobin expression in hybrids which have switched, suggesting that the effect of this compound on ␥-globin expression is due to inhibition of ␥ gene silencing rather than to induction of ␥ gene transcription. Since in other cellular systems, glucocorticoids antagonize the action of butyrate, the effect of dexamethasone on the ␥-to-␤ switch in HFE ؋ MEL hybrids was examined. Dexamethasone strikingly accelerated the ␥-to-␤ switch, and its effect was irreversible. The effects of dexamethasone and butyrate on the ␥-to-␤ switch of the HFE ؋ MEL hybrids appear to be codominant. These results indicate that steroids can have a direct effect on globin gene switching in erythroid cells.

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“…15 In spite of its ability to activate a number of genes, such as the`dormant' fetal g-globin gene, 16 it was also noted that butyrate inhibits the transcriptional activation of several steroid hormone-dependent genes. An inhibitory effect of butyrate was shown for estrogen-mediated gene expression in the chicken oviduct, 17 for glucocorticoiddependent genes in HTC cells, 18,19 in cultured mammary gland fragments 20,21 and for thyroid-mediated gene expression in rat pituitary tumor cells. 22 Interestingly, in rat glioma C6 cells, butyrate was found to block the glucocorticoid-induced increase in glycerol phosphate dehydrogenase 23 but had no effect on glucocorticoid induction of glutamine synthase activity; 24 in HeLa cells the induction of alkaline phosphatase by dexamethasone was, however, potentiated by butyrate.…”

Section: Introductionmentioning

confidence: 99%

Interaction between dexamethasone and butyrate in apoptosis induction: non-additive in thymocytes and synergistic in a T cell-derived leukemia cell line

et al. 1999

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In thymocytes butyrate and trichostatin A are unable to augment dexamethasone-induced apoptosis. In cultured rat thymocytes the extent of apoptosis induced by dexamethasone alone did not increase by addition of 0.1 ± 10 mM butyrate. Even more pronounced was the non-additive interrelationship between dexamethasone and trichostatin A, as trichostatin A-induced apoptosis was not only blocked by the presence of dexamethasone but dexamethasoneinduced apoptosis was also partially inhibited in the presence of 0.1 ± 0.5 mM trichostatin A. The fact that the non-additive relationship with dexamethasone for apoptosis induction was observed with both histone deacetylase inhibitors suggests that in thymocytes this phenomenon is related to histone acetylation. In contrast to this, in the human T cell-derived leukemia cell line CEM-C7H2, dexamethasone did not block butyrate-or trichostatin A-induced apoptosis; moreover, butyrate, in the concentration range of 0.1 ± 1 mM, had a marked synergistic effect on dexamethasone-induced apoptosis. This synergism, however, was not mimicked by trichostatin A, indicating that the effect is not related to histone acetylation but rather due to a pleiotropic effect of butyrate. Furthermore, in CEM-C7H2 cells, at higher concentrations of butyrate (5 ± 10 mM) or trichostatin A (0.4 ± 0.8 mM), there was a minor but reproducible antagonistic effect of dexamethasone on apoptosis induced by each of the two histone deacetylase inhibitors, suggesting that this antagonistic effect too, is related to histone hyperacetylation.

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Selective Inhibition by Sodium Butyrate of Glucorticoid‐Induced Tyrosine Aminotransferase Synthesis in Hepatoma Tissue‐Cultured Cells

Cited by 34 publications

References 53 publications

Control of gene expression by glucocorticoid hormones

Control of gene expression by glucocorticoid hormones

Effects of Butyrate and Glucocorticoids on γ- to β-Globin Gene Switching in Somatic Cell Hybrids

Interaction between dexamethasone and butyrate in apoptosis induction: non-additive in thymocytes and synergistic in a T cell-derived leukemia cell line

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